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Conserved domains on  [gi|835623008|ref|WP_047589287|]
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MULTISPECIES: cupredoxin domain-containing protein [Pseudomonas]

Protein Classification

cupredoxin domain-containing protein( domain architecture ID 10604510)

uncharacterized cupredoxin-like domain-containing protein, similar to CupA, a cell membrane-anchored Cu(I) chaperone involved in copper resistance

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 3-100 5.66e-38

Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel.


:

Pssm-ID: 379208 [Multi-domain]  Cd Length: 104  Bit Score: 123.08  E-value: 5.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835623008    3 CLAVFTFALALPAWSASLPSYELEIRDGHFTPPHLTVPAKQRFKIIVHNRGAGPVEFESLPLRVEKVLGPGVSSFVVIHP 82
Cdd:pfam13473   3 AALAVLFWLSKPAAAADDPTVEITVKDGGFSPSRITVPAGTPVKLEFKNKDKTPAEFESPDLGIEKVLAPGKTSTITIPP 82

                          90
                  ....*....|....*...
gi 835623008   83 LKPGRYTFFDEFHLDLPG 100
Cdd:pfam13473  83 LKPGEYDFFCDMHMDAKG 100
 
Name Accession Description Interval E-value
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 3-100 5.66e-38

Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel.


Pssm-ID: 379208 [Multi-domain]  Cd Length: 104  Bit Score: 123.08  E-value: 5.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835623008    3 CLAVFTFALALPAWSASLPSYELEIRDGHFTPPHLTVPAKQRFKIIVHNRGAGPVEFESLPLRVEKVLGPGVSSFVVIHP 82
Cdd:pfam13473   3 AALAVLFWLSKPAAAADDPTVEITVKDGGFSPSRITVPAGTPVKLEFKNKDKTPAEFESPDLGIEKVLAPGKTSTITIPP 82

                          90
                  ....*....|....*...
gi 835623008   83 LKPGRYTFFDEFHLDLPG 100
Cdd:pfam13473  83 LKPGEYDFFCDMHMDAKG 100
Cupredoxin_like_3 cd04203
Uncharacterized subfamiy of Cupredoxin; Cupredoxins contain type I copper centers and are ...
 24-103 5.88e-13

Uncharacterized subfamiy of Cupredoxin; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. Majority of family members contain multiple cupredoxin domain repeats: ceruloplamin and coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, and spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase and the periplasmic domain of cytochrome c oxidase subunit II. Proteins of this uncharacterized subfamily contain a single cupredoxin domain.


Pssm-ID: 259866 [Multi-domain]  Cd Length: 84  Bit Score: 59.16  E-value: 5.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835623008  24 ELEIRDGHFTPPHLTVPAKQRFKIIVHNRGAGPVEFESLPLRVEKVLGPGVSSFVVIHPLKPGRYTFFDEFHLDLPGGYI 103
Cdd:cd04203    3 KITLNDDYFNPNVITVPINEKTTLILHNKGQKSEETETIKKLGIDVVVESEEINITVKPLSPGTYELICRYHLLG*EGKV 82
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
24-90 6.85e-04

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 36.04  E-value: 6.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835623008  24 ELEIRDGHFTPPHLTVPAKQRFKIIVHNRGAGP----VEFESLplRVEKVLGPGVSSFVVIHPLKPGRYTF 90
Cdd:COG4633   39 TITVDGGGYSPSRITVKAGIPVRLNFTRKDPSGcaeeVVFPDL--GISQDLPLGKTVTIEFTPLKPGEYPF 107
 
Name Accession Description Interval E-value
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 3-100 5.66e-38

Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel.


Pssm-ID: 379208 [Multi-domain]  Cd Length: 104  Bit Score: 123.08  E-value: 5.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835623008    3 CLAVFTFALALPAWSASLPSYELEIRDGHFTPPHLTVPAKQRFKIIVHNRGAGPVEFESLPLRVEKVLGPGVSSFVVIHP 82
Cdd:pfam13473   3 AALAVLFWLSKPAAAADDPTVEITVKDGGFSPSRITVPAGTPVKLEFKNKDKTPAEFESPDLGIEKVLAPGKTSTITIPP 82

                          90
                  ....*....|....*...
gi 835623008   83 LKPGRYTFFDEFHLDLPG 100
Cdd:pfam13473  83 LKPGEYDFFCDMHMDAKG 100
Cupredoxin_like_3 cd04203
Uncharacterized subfamiy of Cupredoxin; Cupredoxins contain type I copper centers and are ...
 24-103 5.88e-13

Uncharacterized subfamiy of Cupredoxin; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. Majority of family members contain multiple cupredoxin domain repeats: ceruloplamin and coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, and spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase and the periplasmic domain of cytochrome c oxidase subunit II. Proteins of this uncharacterized subfamily contain a single cupredoxin domain.


Pssm-ID: 259866 [Multi-domain]  Cd Length: 84  Bit Score: 59.16  E-value: 5.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835623008  24 ELEIRDGHFTPPHLTVPAKQRFKIIVHNRGAGPVEFESLPLRVEKVLGPGVSSFVVIHPLKPGRYTFFDEFHLDLPGGYI 103
Cdd:cd04203    3 KITLNDDYFNPNVITVPINEKTTLILHNKGQKSEETETIKKLGIDVVVESEEINITVKPLSPGTYELICRYHLLG*EGKV 82
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
24-90 6.85e-04

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 36.04  E-value: 6.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835623008  24 ELEIRDGHFTPPHLTVPAKQRFKIIVHNRGAGP----VEFESLplRVEKVLGPGVSSFVVIHPLKPGRYTF 90
Cdd:COG4633   39 TITVDGGGYSPSRITVKAGIPVRLNFTRKDPSGcaeeVVFPDL--GISQDLPLGKTVTIEFTPLKPGEYPF 107
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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